Comparison of the proteome of adult and cord erythroid cells, and changes in the proteome following reticulocyte maturation

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Cord blood stem cells are an attractive starting source for the production of red blood cells in vitro for therapy because of additional expansion potential compared to adult peripheral blood progenitors, and cord blood banks usually being more representative of national populations than blood donors. Consequently it is important to establish how similar cord RBCs are to adult cells. In this study we used Multiplex Tandem Mass Tag labeling combined with nanoLC-MS/MS to compare the proteome of adult and cord RBCs and eticulocytes. 2838 unique proteins were identified, providing the most comprehensive compendium of RBC proteins to date. Using stringent criteria 1674 proteins were quantified, and only a small number differed in amount between adult and cord RBC. We focussed on proteins critical for RBC function. Of these only the expected differences in globin subunits, along with higher levels of carbonic anhydrase 1 & 2 and aquaporin-1 in adult RBCs would be expected to have a phenotypic effect since they are associated with the differences in gaseous exchange between adults and neonates. Since the RBC and reticulocyte samples used were autologous, we catalog the change in proteome following reticulocyte maturation. The majority of proteins (>60% of the 1671 quantified) reduced in abundance between 2 and 100- fold following maturation. However, ~5% were at a higher level in RBCs, localised almost exclusively to cell membranes, in keeping with the known clearance of intracellular recycling pools during reticulocyte maturation. Overall, these data suggest that with respect to the proteome there is no barrier to the use of cord progenitors for the in vitro generation of RBCs for transfusion to adults other than the expression of fetal not adult haemoglobin.
Original languageEnglish
Pages (from-to)1938-1946
Number of pages9
JournalMolecular and Cellular Proteomics
Issue number6
Early online date22 Mar 2016
Publication statusPublished - 1 Jun 2016

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